E4906
Enterokinase from bovine intestine
BioUltra, recombinant, expressed in E. coli, ≥20 units/mg protein, ≥95% (SDS-PAGE)
Sinónimos:
Enteropeptidase
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About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54
Productos recomendados
recombinante
expressed in E. coli
Línea del producto
BioUltra
Análisis
≥95% (SDS-PAGE)
formulario
solution
actividad específica
≥20 units/mg protein
mol peso
150 kDa
envase
vial of ~0.2 unit
concentración
≥0.1 mg/mL
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
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Aplicación
Enterokinase from bovine intestine has been used in a study to assess duodenase as a potential activator of cascade digestive proteases. Enterokinase from bovine intestine has also been used in a study to investigate an inhibitor of enteropeptidases and trypsin from the bovine duodenum.
The enzyme from Sigma has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in Escherichia coli.
Typical conditions for fusion protein cleavage:
Adjust the concentration of the fusion protein to 1.5 mg/ml and a pH between 7.0-8.0 with 500 mM Tris-HCl, pH 8.0, 2.0 mM CaCl2, and 1% Tween® 20
Add enterokinase to fusion protein solution at a ratio of ~ 0.02 units per 1 mg fusion protein and mix
Incubate reaction mixture at ~25 °C for 16 hours
Adjust the concentration of the fusion protein to 1.5 mg/ml and a pH between 7.0-8.0 with 500 mM Tris-HCl, pH 8.0, 2.0 mM CaCl2, and 1% Tween® 20
Add enterokinase to fusion protein solution at a ratio of ~ 0.02 units per 1 mg fusion protein and mix
Incubate reaction mixture at ~25 °C for 16 hours
Enterokinase is a member of the S1 peptidase family. In vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. Enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags.
Acciones bioquímicas o fisiológicas
Enterokinase is a membrane bound serine protease that specifically and rapidly converts trypsinogen to trypsin, thereby, triggering the conversion of other zymogens to active enzymes. It has a molecular mass of approximately 150 kDa. The enzyme is a heterodimer, wherein, the light and the heavy chains are linked by two disulfide bridges. Native enterokinase is composed of an 800 amino acid heavy chain and a 235 amino acid light chain. It is a glycoprotein containing 35% carbohydrate. The polypeptide chain of trypsinogen is hydrolyzed only after an -(Asp)4-Lys- sequence. This cleavage site is incorporated into the FLAG tag. The FLAG® protein expression system is based on the fusion of the 8 amino acid FLAG tag to the recombinant protein of choice. Cleavage by enterokinase removes the FLAG tag from the fusion protein. The enzyme is inhibited by soybean trypsin inhibitor. Enterokinase is typically used in protein modification and amino acid sequence determination.
Propiedades físicas
28 kDa light chain form
Definición de unidad
One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25 °C.
Forma física
supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol
Información legal
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
TWEEN is a registered trademark of Croda International PLC
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Los clientes también vieron
X Zheng et al.
The Journal of biological chemistry, 274(3), 1596-1605 (1999-01-09)
Enteropeptidase is a heterodimeric type II membrane protein of the brush border of duodenal enterocytes. In this location, enteropeptidase cleaves and activates trypsinogen, thereby initiating the activation of other intestinal digestive enzymes. Recombinant bovine enteropeptidase was sorted directly to the
A G Mikhaĭlova et al.
Voprosy meditsinskoi khimii, 44(4), 338-346 (1998-12-10)
Enteropeptidase inhibitor (DI) was isolated from bovine duodenum during purification of this enzyme. DI was purified by affinity chromatography on immobilised trypsin. DI preparations contain two main components: DI-9 (9 kD) and DI-20 (20 kD). The N-terminal amino acid sequence
T S Zamolodchikova et al.
Bioorganicheskaia khimiia, 24(4), 300-305 (1998-06-05)
The substrate specificity of duodenase from bovine duodenum mucosa to synthetic and natural polypeptides was studied. Amino acid residues preferential for duodenase in the P1 and P2 positions of the substrate were determined. It was shown that the enzyme is
Haidong Tan et al.
Protein expression and purification, 56(1), 40-47 (2007-08-21)
The nucleotide sequence encoding bovine enterokinase light chain (EK) from Chinese northern yellow bovine was isolated. Two single-nucleotide mutations, namely, C245G and A528T were identified. The gene encoding the Pro82Arg/Glu176Asp variant of known bovine EK was fused with glutathione S-transferase
Yutetsu Kuruma et al.
Nature protocols, 10(9), 1328-1344 (2015-08-14)
Cell-free gene expression systems are biotechnological tools for the in vitro production of proteins of interest. The addition of membrane vesicles (liposomes) enables the production of membrane proteins, including those in large-molecular-weight complexes, such as the SecYEG translocon or ATP
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